An analysis of incorrectly folded protein models. Implications for structure predictions.

By Jiri Novotny, R. Bruccoleri, M. Karplus. 1984

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

1. Liam J. McGuffin
2. Arne Elofsson
3. Björn Wallner
4. Karolis Uziela
5. David Ménendez Hurtado
6. Ali Hassan Ahmed Maghrabi
7. Claudio Mirabello
8. Keehyoung Joo

Citations in the corpus

• Methods for estimation of model accuracy in CASP12 (2017, methodology): “Motivated by the intriguing experiment of Novotny et al.11 early model accuracy assessment methods focused on distinguishing wrong models (or decoys) from the native structure2,3.”
• Residue-residue potentials with a favorable contact pair term and an unfavorable high packing density term, for simulation and threading. (1996, background): “It was demonstrated that classical semi-empirical potentials such as CHARMM (Brooks et al., 1983) cannot always identify non-native folds of proteins (Novotny et al., 1984).”
• Statistical potentials for fold assessment (2002, unknown): “…Morris et al. 1992; Laskowski et al. 1993, 1998) residue or atom packing density (Gregoret and Cohen 1991), molecular mechanics energy functions (Novotny et al. 1984, 1988; Petrey and Honig 2000), distribution of residues between the solvent accessible and buried positions (Bryant and Am-zel…”